Pathways & interactions
Tissue inhibitor of metalloproteinases-like, OB-fold (IPR008993)
Short name: TIMP-like_OB-fold
- Netrin domain (IPR001134)
- Protease inhibitor I35 (TIMP) (IPR001820)
- Metalloproteinase inhibitor 1 (IPR015611)
- Metalloproteinase inhibitor 3 (IPR015612)
- Metalloproteinase inhibitor 2 (IPR015613)
- Metalloproteinase inhibitor 4 (IPR015614)
- Netrin module, non-TIMP type (IPR018933)
- Proteinase inhibitor I35b (TIMP), C-terminal (IPR027465)
- Tissue inhibitor of metalloproteinase, conserved site (IPR030490)
- Netrin-4, NTR domain (IPR035811)
- Secreted frizzled-related protein 3, NTR domain (IPR035813)
- Procollagen C-endopeptidase enhancer, NTR domain (IPR035814)
- Complement C3-like, NTR domain (IPR035815)
Tissue inhibitors of metalloproteinases (TIMP) are a family of proteins that can form complexes with extracellular matrix metalloproteinases (such as collagenases) and irreversibly inactivate them [PMID: 2793861]. TIMP and related proteins contains a five-stranded antiparallel beta-sheet that is rolled over on itself to form a closed beta-barrel, and two short helices, which pack close to one another on the same barrel face. A comparison of the delta TIMP-2 structure with other known protein folds reveals that the beta-barrel topology is homologous to that seen in proteins of the oligosaccharide/oligonucleotide binding (OB) fold family, a five-stranded beta-sheet coiled to form a closed beta-barrel capped by an alpha-helix located between the third and fourth strands [PMID: 7918391].
Other proteins contain domains with a similar OB-like fold:
- Netrin-like domain (NTR/C345C module), found in procollagen c-proteinase enhancer protein PCOLCE, and in the complement C5 domain.
- Laminin-binding domain, found in agrin.
- SSF50242 (SSF50242)